An EPR investigation of non‐haem iron sites in Escherichia coli bacterioferritin and their interaction with phosphate

FEBS Letters

Harrison, Pauline M.¹  Cheesman, Myles R.²  Andrews, Simon C.¹  Le Brun, Nick E.²  Thomson, Andrew J.²  Moore, Geoffrey R.²  Guest, John R.¹ 

[1] The Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, UK;Centre for Metalloprotein Spectroscopy and Biology, School of Chemical Sciences, University of East Anglia, Norwich NR4 7TJ, UK

关键词: Bacterioferritin (BFR);    NHI site;    Nitric oxide;    Phosphate;   

DOI  :  10.1016/0014-5793(93)81353-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

EPR studies of bacterioferritin (BFR), an iron-storage protein of Escherichia coli [1993, Biochem. J. 292, 47-56.], have revealed the presence of non-haem iron (III) (NHI) sites within the protein coat which may be involved in iron uptake and release. When nitric oxide was used as an EPR spin probe of the Fe(II) state of the NHI sites, two distinct mononuclear NHI species were found. Under certain conditions, an iron dimer was also observed. The reaction of phosphate with NHI species has been investigated. Results point to a function for this anion in core nucleation.

【 授权许可】

Unknown